Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-8-31
pubmed:abstractText
Communication between the 5' cap structure and 3' poly(A) tail of eukaryotic mRNA results in the synergistic enhancement of translation. The cap and poly(A) tail binding proteins, eIF4E and Pab1p, mediate this effect in the yeast S. cerevisiae through their interactions with different parts of the translation factor eIF4G. Here, we demonstrate the reconstitution of an eIF4E/eIF4G/Pab1p complex with recombinant proteins, and show by atomic force microscopy that the complex can circularize capped, polyadenylated RNA. Our results suggest that formation of circular mRNA by translation factors could contribute to the control of mRNA expression in the eukaryotic cell.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4E, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4G, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors, http://linkedlifedata.com/resource/pubmed/chemical/Poly(A)-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, circular, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TIF4631 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
135-40
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9702200-Eukaryotic Initiation Factor-4E, pubmed-meshheading:9702200-Eukaryotic Initiation Factor-4G, pubmed-meshheading:9702200-Fungal Proteins, pubmed-meshheading:9702200-Glutathione Transferase, pubmed-meshheading:9702200-Macromolecular Substances, pubmed-meshheading:9702200-Microscopy, Atomic Force, pubmed-meshheading:9702200-Nucleic Acid Conformation, pubmed-meshheading:9702200-Peptide Fragments, pubmed-meshheading:9702200-Peptide Initiation Factors, pubmed-meshheading:9702200-Poly(A)-Binding Proteins, pubmed-meshheading:9702200-Protein Biosynthesis, pubmed-meshheading:9702200-RNA, pubmed-meshheading:9702200-RNA, Fungal, pubmed-meshheading:9702200-RNA, Messenger, pubmed-meshheading:9702200-RNA-Binding Proteins, pubmed-meshheading:9702200-Recombinant Fusion Proteins, pubmed-meshheading:9702200-Saccharomyces cerevisiae, pubmed-meshheading:9702200-Saccharomyces cerevisiae Proteins
pubmed:year
1998
pubmed:articleTitle
Circularization of mRNA by eukaryotic translation initiation factors.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't